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Conserved domains on  [gi|1778635129|ref|WP_154830098|]
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glycosyltransferase [Dietzia kunjamensis]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 11-404 4.16e-60

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03802:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 333  Bit Score: 198.28  E-value: 4.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  11 IAVIGPSRFPIREPYAGGLEVVVAKEVRALRARGHRVTLYAAAGSEGHDRrhefttLAAATGRGDSYYPPGGYEADAAEF 90
Cdd:cd03802     2 IAQVSPPRGPVPPGKYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAP------LVAVIPRALRLDPIPQESKLAELL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  91 ERLMDHVAVSGFDVVLNHSLsHVPLVRAAEMATPMITTLHCPQLAPMQEAFDRLgsATGRVLAVSHSVLGSWRVPHGAEV 170
Cdd:cd03802    76 EALEVQLRASDFDVIHNHSY-DWLPPFAPLIGTPFVTTLHGPSIPPSLAIYAAE--PPVNYVSISDAQRAATPPIDYLTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 171 LPNGVDLQVWRPragaagrtaarsaarsafrpaagtagtaataaaarpvagrtsrvglRPTDRPRAVWTGRIVPEKGPHL 250
Cdd:cd03802   153 VHNGLDPADYRF----------------------------------------------QPDPEDYLAFLGRIAPEKGLED 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 251 AVEAARRTGLRLDLAGRVGDDRYMERVLAPRLrdaGDSVRYHGPLGRDALVPLVASVAVALVTPCWEEPFGLTAIEALAC 330
Cdd:cd03802   187 AIRVARRAGLPLKIAGKVRDEDYFYYLQEPLP---GPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMAC 263

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 331 GTPVVALARGGIREILsgQPGVV--LVEPGrdpaSALAASIPAALTLDRAATARAAAAAFSHDARIDLLEARLRGL 404
Cdd:cd03802   264 GTPVIAYRRGGLPEVI--QHGETgfLVDSV----EEMAEAIANIDRIDRAACRRYAEDRFSAARMADRYEALYRKV 333
 
Name Accession Description Interval E-value
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 11-404 4.16e-60

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 198.28  E-value: 4.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  11 IAVIGPSRFPIREPYAGGLEVVVAKEVRALRARGHRVTLYAAAGSEGHDRrhefttLAAATGRGDSYYPPGGYEADAAEF 90
Cdd:cd03802     2 IAQVSPPRGPVPPGKYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAP------LVAVIPRALRLDPIPQESKLAELL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  91 ERLMDHVAVSGFDVVLNHSLsHVPLVRAAEMATPMITTLHCPQLAPMQEAFDRLgsATGRVLAVSHSVLGSWRVPHGAEV 170
Cdd:cd03802    76 EALEVQLRASDFDVIHNHSY-DWLPPFAPLIGTPFVTTLHGPSIPPSLAIYAAE--PPVNYVSISDAQRAATPPIDYLTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 171 LPNGVDLQVWRPragaagrtaarsaarsafrpaagtagtaataaaarpvagrtsrvglRPTDRPRAVWTGRIVPEKGPHL 250
Cdd:cd03802   153 VHNGLDPADYRF----------------------------------------------QPDPEDYLAFLGRIAPEKGLED 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 251 AVEAARRTGLRLDLAGRVGDDRYMERVLAPRLrdaGDSVRYHGPLGRDALVPLVASVAVALVTPCWEEPFGLTAIEALAC 330
Cdd:cd03802   187 AIRVARRAGLPLKIAGKVRDEDYFYYLQEPLP---GPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMAC 263

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 331 GTPVVALARGGIREILsgQPGVV--LVEPGrdpaSALAASIPAALTLDRAATARAAAAAFSHDARIDLLEARLRGL 404
Cdd:cd03802   264 GTPVIAYRRGGLPEVI--QHGETgfLVDSV----EEMAEAIANIDRIDRAACRRYAEDRFSAARMADRYEALYRKV 333
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 232-369 3.21e-20

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 86.56  E-value: 3.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 232 DRPRAVWTGRIVPEKGPHLAVEAARR-----TGLRLDLAGRvGDDRYMERVLApRLRDAGDSVRYHGPLGRDALVPLVAS 306
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALlkeknPNLKLVIAGD-GEEEKRLKKLA-EKLGLGDNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778635129 307 vAVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREIL-SGQPGvVLVEPGRdpASALAASI 369
Cdd:pfam00534  79 -ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkDGETG-FLVKPNN--AEALAEAI 138
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 296-405 1.93e-10

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 58.08  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 296 GRDALVPLVASVAVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREILSGQPGVVLVEPGrDPAsALAASI------ 369
Cdd:COG0438     9 GLDLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPG-DPE-ALAEAIlrlled 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1778635129 370 PAALTLDRAATARAAAAAFSHDARIDLLEARLRGLL 405
Cdd:COG0438    87 PELRRRLGEAARERAEERFSWEAIAERLLALYEELL 122
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 38-392 1.84e-06

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 49.70  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  38 RALRARGHRVTLYA-AAGSEGHDR--RHEFTTLAAATGRGDSyypPGGYEADAAEFERLMDHVAVSGFDVVLNH---SLS 111
Cdd:TIGR04047  23 EALTALGHDVTVWAlAADGFGFFRdpPCAVRLVPVAPAPGDT---DAMVEQRIARSIDHLRAHFARGFDVVHAQdciSGN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 112 HVPLVRAAEMATPMITTLH------CPQLAPMQEafdRLGSATGRVLAVSHSVLGSWRVPHG--AEVLPNGVDLQVWRPR 183
Cdd:TIGR04047 100 ALATLRAEGLIPGFVRTVHhlddfdDPRLAACQE---RAIVEADAVLCVSAAWAAELRAEWGidATVVPNGVDAARFSPA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 184 AGAagrtaarsaarsafrpaagtagtaataaaaRPVAGRTsRVGLRPTDRPRAVwtGRIVPEKGPHLAVEA-----ARRT 258
Cdd:TIGR04047 177 ADA------------------------------ADAALRR-RLGLRGGPYVLAV--GGIEPRKNTIDLLEAfallrARRP 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 259 GLRLDLAG---RVGDDRYMERVLApRLRDAGDSVRYH---GPLGRDALVPLVASvAVALVTPCWEEPFGLTAIEALACGT 332
Cdd:TIGR04047 224 QAQLVIAGgatLFDYDAYRREFRA-RAAELGVDPGPVvitGPVPDADLPALYRC-ADAFAFPSLKEGFGLVVLEALASGI 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 333 PVVALARGGIREILSGQPGVVlvepgRDP------ASALAASIPAALTLDRAATARAAAAAFSHDA 392
Cdd:TIGR04047 302 PVVASDIAPFTEYLGRFDAAW-----ADPsdpdsiADALALALDPARRPALRAAGPELAARYTWDA 362
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
230-357 1.68e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 46.71  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 230 PTDRPRAVWTGRIVPEKGPHLAVEA-----ARRTGLRLDLAG-----RVGDD-RYMERVL--APRLRDAGDSVRYHGPLG 296
Cdd:PRK15484  190 SPDETVLLYAGRISPDKGILLLMQAfeklaTAHSNLKLVVVGdptasSKGEKaAYQKKVLeaAKRIGDRCIMLGGQPPEK 269

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778635129 297 RDALVPLvasvAVALVTPC-WEEPFGLTAIEALACGTPVVALARGGIRE-ILSGQPGVVLVEP 357
Cdd:PRK15484  270 MHNYYPL----ADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEfVLEGITGYHLAEP 328
 
Name Accession Description Interval E-value
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 11-404 4.16e-60

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 198.28  E-value: 4.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  11 IAVIGPSRFPIREPYAGGLEVVVAKEVRALRARGHRVTLYAAAGSEGHDRrhefttLAAATGRGDSYYPPGGYEADAAEF 90
Cdd:cd03802     2 IAQVSPPRGPVPPGKYGGTELVVSALTEGLVRRGHEVTLFAPGDSHTSAP------LVAVIPRALRLDPIPQESKLAELL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  91 ERLMDHVAVSGFDVVLNHSLsHVPLVRAAEMATPMITTLHCPQLAPMQEAFDRLgsATGRVLAVSHSVLGSWRVPHGAEV 170
Cdd:cd03802    76 EALEVQLRASDFDVIHNHSY-DWLPPFAPLIGTPFVTTLHGPSIPPSLAIYAAE--PPVNYVSISDAQRAATPPIDYLTV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 171 LPNGVDLQVWRPragaagrtaarsaarsafrpaagtagtaataaaarpvagrtsrvglRPTDRPRAVWTGRIVPEKGPHL 250
Cdd:cd03802   153 VHNGLDPADYRF----------------------------------------------QPDPEDYLAFLGRIAPEKGLED 186

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 251 AVEAARRTGLRLDLAGRVGDDRYMERVLAPRLrdaGDSVRYHGPLGRDALVPLVASVAVALVTPCWEEPFGLTAIEALAC 330
Cdd:cd03802   187 AIRVARRAGLPLKIAGKVRDEDYFYYLQEPLP---GPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMAC 263

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 331 GTPVVALARGGIREILsgQPGVV--LVEPGrdpaSALAASIPAALTLDRAATARAAAAAFSHDARIDLLEARLRGL 404
Cdd:cd03802   264 GTPVIAYRRGGLPEVI--QHGETgfLVDSV----EEMAEAIANIDRIDRAACRRYAEDRFSAARMADRYEALYRKV 333
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 11-374 1.87e-33

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 128.42  E-value: 1.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  11 IAVIGPSRFPirepYAGGLEVVVAKEVRALRARGHRVTLYAAAGSEGHDRRHEFTtlaaatGRGDSYYPPGGYEADAAEF 90
Cdd:cd03801     2 ILLLSPELPP----PVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDG------VIVPLLPSLAALLRARRLL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  91 ERLMDHVAVSGFDVVLNHSLSHVPLVRAAEMA--TPMITTLHC-----------PQLAPMQEAFDRLGSATgRVLAVSHS 157
Cdd:cd03801    72 RELRPLLRLRKFDVVHAHGLLAALLAALLALLlgAPLVVTLHGaepgrlllllaAERRLLARAEALLRRAD-AVIAVSEA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 158 VLGSWR-----VPHGAEVLPNGVDLQVWRPRAGAAGrtaarsaarsafrpaagtagtaataaaarpvagrtsrvgLRPTD 232
Cdd:cd03801   151 LRDELRalggiPPEKIVVIPNGVDLERFSPPLRRKL---------------------------------------GIPPD 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 233 RPRAVWTGRIVPEKGPHLAVEAA-----RRTGLRLDLAGRVGDDRymeRVLAPRLRDAGDSVRYHGPLGRDALVPLVASv 307
Cdd:cd03801   192 RPVLLFVGRLSPRKGVDLLLEALakllrRGPDVRLVIVGGDGPLR---AELEELELGLGDRVRFLGFVPDEELPALYAA- 267

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778635129 308 AVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREILSGQPGVVLVEPgrDPASALAASIPAALT 374
Cdd:cd03801   268 ADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPP--DDVEALADALLRLLA 332
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 24-374 3.59e-23

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 99.71  E-value: 3.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  24 PYAGGLEVVVAKEVRALRARGHRVTLYAAaGSEGHDRRHEFTTLAAATGRGDSYYPPGGY-----------EADAAEFER 92
Cdd:cd03823    12 QRVGGAEISVHDLAEALVAEGHEVAVLTA-GVGPPGQATVARSVVRYRRAPDETLPLALKrrgyelfetynPGLRRLLAR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  93 LMDHVavsGFDVVLNHSLS--HVPLVRAA-EMATPMITTLH-CPQLAPMQEAFDRLGSAtgrVLAVSHSVLGSWRVpHGA 168
Cdd:cd03823    91 LLEDF---RPDVVHTHNLSglGASLLDAArDLGIPVVHTLHdYWLLCPRQFLFKKGGDA---VLAPSRFTANLHEA-NGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 169 -----EVLPNGVDlqvwrpragaagrtaarsaarsafrpaagtagtaatAAAARPVAGRtsrvglRPTDRPRAVWTGRIV 243
Cdd:cd03823   164 fsariSVIPNAVE------------------------------------PDLAPPPRRR------PGTERLRFGYIGRLT 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 244 PEKGPHLAVEAAR---RTGLRLDLAGRVGDDRYmervlapRLRDAGDSVRYHGPLGRDALVPLVASVAVALVTPCWEEPF 320
Cdd:cd03823   202 EEKGIDLLVEAFKrlpREDIELVIAGHGPLSDE-------RQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPF 274

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1778635129 321 GLTAIEALACGTPVVALARGGIREILSGQPGVVLVEPGrdPASALAASIPAALT 374
Cdd:cd03823   275 GLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPG--DAEDLAAAMRRLLT 326
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 232-369 3.21e-20

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 86.56  E-value: 3.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 232 DRPRAVWTGRIVPEKGPHLAVEAARR-----TGLRLDLAGRvGDDRYMERVLApRLRDAGDSVRYHGPLGRDALVPLVAS 306
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALlkeknPNLKLVIAGD-GEEEKRLKKLA-EKLGLGDNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778635129 307 vAVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREIL-SGQPGvVLVEPGRdpASALAASI 369
Cdd:pfam00534  79 -ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkDGETG-FLVKPNN--AEALAEAI 138
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 228-369 8.74e-19

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 87.30  E-value: 8.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 228 LRPTDRPRAVWTGRIVPEKGPHLAVEA-----ARRTGLRLDLAG-----RVGDDRYMERVLAPRLRdAGDSVRYHGPLGR 297
Cdd:cd03800   215 LLPPDKPVVLALGRLDPRKGIDTLVRAfaqlpELRELANLVLVGgpsddPLSMDREELAELAEELG-LIDRVRFPGRVSR 293

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778635129 298 DALvPLVASVAVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREILS-GQPGvVLVePGRDPAsALAASI 369
Cdd:cd03800   294 DDL-PELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRdGRTG-LLV-DPHDPE-ALAAAL 362
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
233-369 1.24e-18

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 81.79  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 233 RPRAVWTGRIVPE-KGPHLAVEA-----ARRTGLRLDLAGRvGDDRYMERvlapRLRDAGDSVRYHGPlgRDALVPLVAS 306
Cdd:pfam13692   1 RPVILFVGRLHPNvKGVDYLLEAvpllrKRDNDVRLVIVGD-GPEEELEE----LAAGLEDRVIFTGF--VEDLAELLAA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778635129 307 VAVALVtPCWEEPFGLTAIEALACGTPVVALARGGIREILSGQPGvVLVEPGrDPAsALAASI 369
Cdd:pfam13692  74 ADVFVL-PSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENG-LLVPPG-DPE-ALAEAI 132
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 27-369 2.74e-18

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 85.49  E-value: 2.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  27 GGLEVVVAKEVRALRARGHRVTLYAAAGsEGHDRRHEFTTLAAATGRGDSYYPPGGyeADAAEFERLMDHVAVSGFDVVL 106
Cdd:cd03811    12 GGAERVLLNLANALDKRGYDVTLVLLRD-EGDLDKQLNGDVKLIRLLIRVLKLIKL--GLLKAILKLKRILKRAKPDVVI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 107 NHSLSHVPLVR-AAEMATPMITTLHC-PQLAPMQEAFDRLGSATGR----VLAVSHSVLGS-----WRVPHGAEVLPNGV 175
Cdd:cd03811    89 SFLGFATYIVAkLAAARSKVIAWIHSsLSKLYYLKKKLLLKLKLYKkadkIVCVSKGIKEDlirlgPSPPEKIEVIYNPI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 176 DLQvwrpragaagrtaarsaarsafrpaagtagtaataaaaRPVAGRTSRVGLRPTDRPRAVWTGRIVPEKGPHLAVEAA 255
Cdd:cd03811   169 DID--------------------------------------RIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAF 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 256 RR-----TGLRLDLAGrVGDDRYMERVLAPRLrDAGDSVRYHGPlgRDALVPLVASvAVALVTPCWEEPFGLTAIEALAC 330
Cdd:cd03811   211 AKlrkkyPDVKLVILG-DGPLREELEKLAKEL-GLAERVIFLGF--QSNPYPYLKK-ADLFVLSSRYEGFPNVLLEAMAL 285

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1778635129 331 GTPVVALARGGIREILSGQPGVVLVEPgrDPASALAASI 369
Cdd:cd03811   286 GTPVVSTDCPGPREILDDGENGLLVPD--GDAAALAGIL 322
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 23-376 1.47e-17

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 83.17  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  23 EPYAGGLEVVVAKEVRALRARGHRVTLYAAAGSEGHDRRHEFTTLAAATGRGDSYYPPggyeadaaeFERLMDHVAVSGF 102
Cdd:cd03819     7 ALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPLLRALLG---------NVRLARLIRRERI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 103 DVVLNHSLSHVPLVRAAE--MATPMITTLHCPQLAPMQEAFDRLGS--ATGRVLAVSHSV----LGSWRVPHGA-EVLPN 173
Cdd:cd03819    78 DLIHAHSRAPAWLGWLASrlTGVPLVTTVHGSYLATYHPKDFALAVraRGDRVIAVSELVrdhlIEALGVDPERiRVIPN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 174 GVDLQVWRPragaagrtaarsaarsafrpaagtagtaataaaaRPVAGRTSRVGLrPTDRPRAVWTGRIVPEKGPHLAVE 253
Cdd:cd03819   158 GVDTDRFPP----------------------------------EAEAEERAQLGL-PEGKPVVGYVGRLSPEKGWLLLVD 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 254 AA----RRTGLRLDLAGRVGDDRYMERVLAPRLRDagDSVRYHGPlgRDALVPLVASVAVaLVTPCWEEPFGLTAIEALA 329
Cdd:cd03819   203 AAaelkDEPDFRLLVAGDGPERDEIRRLVERLGLR--DRVTFTGF--REDVPAALAASDV-VVLPSLHEEFGRVALEAMA 277

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1778635129 330 CGTPVVALARGGIREIL-SGQPGVVLVEPGRDpasALAASIPAALTLD 376
Cdd:cd03819   278 CGTPVVATDVGGAREIVvHGRTGLLVPPGDAE---ALADAIRAAKLLP 322
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 225-376 6.55e-17

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 81.57  E-value: 6.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 225 RVGLRPTDRPRAVWTGRIVPEKGPHLAVEAARR----TGLRLDLagrVGDDRYmervlAPRLRDAGDSVRYHGPLGRDAL 300
Cdd:cd03814   190 RRRLGPPGRPLLLYVGRLAPEKNLEALLDADLPlaasPPVRLVV---VGDGPA-----RAELEARGPDVIFTGFLTGEEL 261

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 301 VPLVASvAVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREILSGQPGVVLVEPGRDPASALAAsipAALTLD 376
Cdd:cd03814   262 ARAYAS-ADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAAL---RALLED 333
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 27-373 6.15e-16

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 78.58  E-value: 6.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  27 GGLEVVVAKEVRALRARGHRVTLYAAA----GSEGHDRRHEFTTLAAATGRGDSYYPPGGYEADAAEFERLMDHVAVSG- 101
Cdd:cd03798    14 PGRGIFVRRQVRALSRRGVDVEVLAPApwgpAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSLAKLLKRRRr 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 102 --FDVVLNHSLSHVPLV---RAAEMATPMITTLHC------PQLAPMQEAFDR-LGSATgRVLAVSHSV------LGSWR 163
Cdd:cd03798    94 gpPDLIHAHFAYPAGFAaalLARLYGVPYVVTEHGsdinvfPPRSLLRKLLRWaLRRAA-RVIAVSKALaeelvaLGVPR 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 164 VPhgAEVLPNGVDLQVWRPragaagrtaarsaarsafrpaagtagtaataaaarpvagRTSRVGLrPTDRPRAVWTGRIV 243
Cdd:cd03798   173 DR--VDVIPNGVDPARFQP---------------------------------------EDRGLGL-PLDAFVILFVGRLI 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 244 PEKGPHLAVEA-----ARRTGLRLDLAGRVGDDRYMERVLAPRLRDAGdsVRYHGPLGRDAlVPLVASVAVALVTPCWEE 318
Cdd:cd03798   211 PRKGIDLLLEAfarlaKARPDVVLLIVGDGPLREALRALAEDLGLGDR--VTFTGRLPHEQ-VPAYYRACDVFVLPSRHE 287

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1778635129 319 PFGLTAIEALACGTPVVALARGGIREILSGQPGVVLVEPGRdpASALAASIPAAL 373
Cdd:cd03798   288 GFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGD--ADALAAALRRAL 340
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 235-355 2.07e-15

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 75.13  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 235 RAVWTGRIVPEKGPHLAVEA-----ARRTGLRLDLAGRVGDDRYMERVLAprLRDAGDSVRYHGPLGRDALVPLVASVAV 309
Cdd:cd01635   112 DKVSVGRLVPEKGIDLLLEAlallkARLPDLVLVLVGGGGEREEEEALAA--ALGLLERVVIIGGLVDDEVLELLLAAAD 189

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1778635129 310 ALVTPCWEEPFGLTAIEALACGTPVVALARGGIREILSGQPGVVLV 355
Cdd:cd01635   190 VFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 240-367 2.82e-14

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 73.47  E-value: 2.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 240 GRIVPEKGPHLAVEAARRTGLRLDLagrVGDDRYMERvlaprLRD-AGDSVRYHGPLGRDALVPLVASvAVALVTPCwEE 318
Cdd:cd03804   206 SRLVPYKRIDLAVEAFNELPKRLVV---IGDGPDLDR-----LRAmASPNVEFLGYQPDEVLKELLSK-ARAFVFAA-EE 275

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1778635129 319 PFGLTAIEALACGTPVVALARGGIRE-ILSGQPGVVLVEpgRDPASALAA 367
Cdd:cd03804   276 DFGIVPVEAQACGTPVIAFGKGGALEtVRPGPTGILFGE--QTVESLKAA 323
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 23-376 1.34e-13

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 71.54  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  23 EPYAGGLEVVVAKEVRALRARGHRVTLYAAAgSEGHDRRHEFTTLAAATGRGDSYYPPGGYEADAaefERLMDHVAVSGF 102
Cdd:cd03817    10 LPQVNGVATSVRNLARALEKRGHEVYVITPS-DPGAEDEEEVVRYRSFSIPIRKYHRQHIPFPFK---KAVIDRIKELGP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 103 DVVlnHSlsHVPLVR-------AAEMATPMITTLHCP-----QLAPMQEAFD---------RLGSATGRVLAVSHSVLGS 161
Cdd:cd03817    86 DII--HT--HTPFSLgklglriARKLKIPIVHTYHTMyedylHYIPKGKLLVkavvrklvrRFYNHTDAVIAPSEKIKDT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 162 WR-----VPhgAEVLPNGVDLQVWRPRAgaagrtaarsaarsafrpaagtagtaataaaarPVAGRTSRvGLRPtDRPRA 236
Cdd:cd03817   162 LReygvkGP--IEVIPNGIDLDKFEKPL---------------------------------NTEERRKL-GLPP-DEPIL 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 237 VWTGRIVPEKGPHLAVEAARR----TGLRLDLAGRvGDDR-YMERvLAPRLrDAGDSVRYHGPLGRDaLVPLVASVAVAL 311
Cdd:cd03817   205 LYVGRLAKEKNIDFLLRAFAElkkePNIKLVIVGD-GPEReELKE-LAREL-GLADKVIFTGFVPRE-ELPEYYKAADLF 280

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 312 VTPCWEEPFGLTAIEALACGTPVVALARGGIRE-ILSGQPGvVLVEPGRDPASALAASIPAALTLD 376
Cdd:cd03817   281 VFASTTETQGLVYLEAMAAGLPVVAAKDPAASElVEDGENG-FLFEPNDETLAEKLLHLRENLELL 345
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 278-369 5.73e-11

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 63.50  E-value: 5.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 278 LAPRLRDAGDSVRYHGPLGRDALVPLVASVAVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREILsgQPGVV--LV 355
Cdd:cd03825   234 NDPQIVILPFDIISLGYIDDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIV--QHGVTgyLV 311

                          90
                  ....*....|....
gi 1778635129 356 EPGrDPAsALAASI 369
Cdd:cd03825   312 PPG-DVQ-ALAEAI 323
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 24-373 5.85e-11

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 63.54  E-value: 5.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  24 PYAGGLEVVVAKEVRALRARGHRVTLY--AAAGSEGHDRRHEFTTLAAATGRGDSYYPPGGYEADAAEFERLMDHVAVSG 101
Cdd:cd03821    11 PKAGGPVKVVLRLAAALAALGHEVTIVstGDGYESLVVEENGRYIPPQDGFASIPLLRQGAGRTDFSPGLPNWLRRNLRE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 102 FDVVLNHSLSHVPLVRAAEMA----TPMITTLH---CPQLAPMQEAFDRL-----------GSATGRVLAVSHSVLGSWR 163
Cdd:cd03821    91 YDVVHIHGVWTYTSLAACKLArrrgIPYVVSPHgmlDPWALQQKHWKKRIalhlierrnlnNAALVHFTSEQEADELRRF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 164 VPHGAE-VLPNGVDLQVWrpragaagrtaarsaarsafrpaagtagtaataaaarPVAGRTSRVGLRPTDRPRAVWTGRI 242
Cdd:cd03821   171 GLEPPIaVIPNGVDIPEF-------------------------------------DPGLRDRRKHNGLEDRRIILFLGRI 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 243 VPEKGPHLAVEAARR---TGLRLDLAgRVGDDRYMERVLAPRLRDAG--DSVRYHGPLGRDALVPLVASvAVALVTPCWE 317
Cdd:cd03821   214 HPKKGLDLLIRAARKlaeQGRDWHLV-IAGPDDGAYPAFLQLQSSLGlgDRVTFTGPLYGEAKWALYAS-ADLFVLPSYS 291

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 318 EPFGLTAIEALACGTPVVALARGGIREILSGQPGVVlvepGRDPASALAASIPAAL 373
Cdd:cd03821   292 ENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVV----VDPNVSSLAEALAEAL 343
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 296-405 1.93e-10

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 58.08  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 296 GRDALVPLVASVAVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREILSGQPGVVLVEPGrDPAsALAASI------ 369
Cdd:COG0438     9 GLDLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPG-DPE-ALAEAIlrlled 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1778635129 370 PAALTLDRAATARAAAAAFSHDARIDLLEARLRGLL 405
Cdd:COG0438    87 PELRRRLGEAARERAEERFSWEAIAERLLALYEELL 122
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 230-369 3.25e-10

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 61.07  E-value: 3.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 230 PTDRPRAVWTGRIVPEKGPHLAVEAARR-----TGLRLDLAGrvGDDRYMERVLAPRLRDAGDSVRYHGPlgRDALVPLV 304
Cdd:cd03808   186 PSEKVVFLFVARLLKDKGIDELIEAAKIlkkkgPNVRFLLVG--DGELENPSEILIEKLGLEGRIEFLGF--RSDVPELL 261

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 305 ASVAVaLVTPCWEEPFGLTAIEALACGTPVVALARGGIRE-ILSGQPGvVLVEPGrDPAsALAASI 369
Cdd:cd03808   262 AESDV-FVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRElVIDGVNG-FLVPPG-DVE-ALADAI 323
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 25-373 8.63e-10

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 60.02  E-value: 8.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  25 YAGGLEVVVAKEVRALRARGHRVTLYAAAGseghdRRHEFTTLAAAtgrGDSYYPPGG-YEADAAEFERLMDHVAVSGFD 103
Cdd:cd03807    10 NVGGAETMLLRLLEHMDKSRFEHVVISLTG-----DGVLGEELLAA---GVPVVCLGLsSGKDPGVLLRLAKLIRKRNPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 104 VV---LNHSLSHVPLvrAAEMA--TPMITTLHC----PQLAPMQEAFDRLGSATGRV-LAVSHSVLGS----WRVPHGAE 169
Cdd:cd03807    82 VVhtwMYHADLIGGL--AAKLAggVKVIWSVRSsnipQRLTRLVRKLCLLLSKFSPAtVANSSAVAEFhqeqGYAKNKIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 170 VLPNGVDLQVWRPRAGAAGRTAarsaarsafrpaagtagtaataaaarpvagrtSRVGLrPTDRPRAVWTGRIVPEKGPH 249
Cdd:cd03807   160 VIYNGIDLFKLSPDDASRARAR--------------------------------RRLGL-AEDRRVIGIVGRLHPVKDHS 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 250 LAVEAAR-----RTGLRLDLAGRVGddrymERVLAPRLRDA---GDSVRYHGPLGRdalVPLVASVAVALVTPCWEEPFG 321
Cdd:cd03807   207 DLLRAAAllvetHPDLRLLLVGRGP-----ERPNLERLLLElglEDRVHLLGERSD---VPALLPAMDIFVLSSRTEGFP 278

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1778635129 322 LTAIEALACGTPVVALARGGIREILSGQPGVvlVEPGRDPAsALAASIPAAL 373
Cdd:cd03807   279 NALLEAMACGLPVVATDVGGAAELVDDGTGF--LVPAGDPQ-ALADAIRALL 327
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
27-178 4.30e-09

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 55.23  E-value: 4.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  27 GGLEVVVAKEVRALRARGHRVTLYAAagseGHDRRHEFTTLAAATGRGDSYYPPGGYEADAAEFERLMDHVAVSGFDVVL 106
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTP----GGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 107 NH---SLSHVPLVRAAEMATPMITTLHC-------------PQLAPMQEAFDRLGSATGRVLAVSHSVLGSWRVPHGA-- 168
Cdd:pfam13439  77 AHspfPLGLAALAARLRLGIPLVVTYHGlfpdykrlgarlsPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVpp 156

                         170
                  ....*....|...
gi 1778635129 169 ---EVLPNGVDLQ 178
Cdd:pfam13439 157 ekiRVIPNGVDLE 169
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 229-373 1.86e-08

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 55.92  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 229 RPTDRPRAVWTGRIVPEKGPHLAVEAARRtglrldLAGRVGDDRYM---ERVLAPRLRD---AGDSVRYHGPLGRDALVP 302
Cdd:cd05844   185 PAERAPTILFVGRLVEKKGCDVLIEAFRR------LAARHPTARLViagDGPLRPALQAlaaALGRVRFLGALPHAEVQD 258

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778635129 303 LVASvAVALVTPCW------EEPFGLTAIEALACGTPVVALARGGIRE-ILSGQPGvvLVEPGRDPAsALAASIPAAL 373
Cdd:cd05844   259 WMRR-AEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEaILDGETG--FLVPEGDVD-ALADALQALL 332
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 240-369 5.29e-08

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 54.29  E-value: 5.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 240 GRIVPEKGPHLAVEAARR-----TGLRLDLAGRvGDDRYMERVLAPRLRDAGDSVRYhgpLGR--DALVPLVASVAVALV 312
Cdd:cd03809   199 GTLEPRKNHERLLKAFALlkkqgGDLKLVIVGG-KGWEDEELLDLVKKLGLGGRVRF---LGYvsDEDLPALYRGARAFV 274

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1778635129 313 TPCWEEPFGLTAIEALACGTPVVALARGGIREIlsGQPGVVLVEPgRDPaSALAASI 369
Cdd:cd03809   275 FPSLYEGFGLPVLEAMACGTPVIASNISVLPEV--AGDAALYFDP-LDP-ESIADAI 327
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 38-392 1.84e-06

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 49.70  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129  38 RALRARGHRVTLYA-AAGSEGHDR--RHEFTTLAAATGRGDSyypPGGYEADAAEFERLMDHVAVSGFDVVLNH---SLS 111
Cdd:TIGR04047  23 EALTALGHDVTVWAlAADGFGFFRdpPCAVRLVPVAPAPGDT---DAMVEQRIARSIDHLRAHFARGFDVVHAQdciSGN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 112 HVPLVRAAEMATPMITTLH------CPQLAPMQEafdRLGSATGRVLAVSHSVLGSWRVPHG--AEVLPNGVDLQVWRPR 183
Cdd:TIGR04047 100 ALATLRAEGLIPGFVRTVHhlddfdDPRLAACQE---RAIVEADAVLCVSAAWAAELRAEWGidATVVPNGVDAARFSPA 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 184 AGAagrtaarsaarsafrpaagtagtaataaaaRPVAGRTsRVGLRPTDRPRAVwtGRIVPEKGPHLAVEA-----ARRT 258
Cdd:TIGR04047 177 ADA------------------------------ADAALRR-RLGLRGGPYVLAV--GGIEPRKNTIDLLEAfallrARRP 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 259 GLRLDLAG---RVGDDRYMERVLApRLRDAGDSVRYH---GPLGRDALVPLVASvAVALVTPCWEEPFGLTAIEALACGT 332
Cdd:TIGR04047 224 QAQLVIAGgatLFDYDAYRREFRA-RAAELGVDPGPVvitGPVPDADLPALYRC-ADAFAFPSLKEGFGLVVLEALASGI 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 333 PVVALARGGIREILSGQPGVVlvepgRDP------ASALAASIPAALTLDRAATARAAAAAFSHDA 392
Cdd:TIGR04047 302 PVVASDIAPFTEYLGRFDAAW-----ADPsdpdsiADALALALDPARRPALRAAGPELAARYTWDA 362
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
230-357 1.68e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 46.71  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 230 PTDRPRAVWTGRIVPEKGPHLAVEA-----ARRTGLRLDLAG-----RVGDD-RYMERVL--APRLRDAGDSVRYHGPLG 296
Cdd:PRK15484  190 SPDETVLLYAGRISPDKGILLLMQAfeklaTAHSNLKLVVVGdptasSKGEKaAYQKKVLeaAKRIGDRCIMLGGQPPEK 269

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778635129 297 RDALVPLvasvAVALVTPC-WEEPFGLTAIEALACGTPVVALARGGIRE-ILSGQPGVVLVEP 357
Cdd:PRK15484  270 MHNYYPL----ADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEfVLEGITGYHLAEP 328
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 240-369 1.78e-05

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 46.46  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 240 GRIVPEKGPHLAVEAARRT-----GLRLDLAGrVGDDRYMERVLAPRLrDAGDSVRYHGPLGRDALVPLVASVAValVTP 314
Cdd:cd03820   188 GRLTYQKGFDLLIEAWALIakkhpDWKLRIYG-DGPEREELEKLIDKL-GLEDRVKLLGPTKNIAEEYANSSIFV--LSS 263

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1778635129 315 CWEEpFGLTAIEALACGTPVVALAR-GGIREILSGQPGVVLVEPGRdpASALAASI 369
Cdd:cd03820   264 RYEG-FPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPNGD--VDALAEAL 316
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 240-369 2.01e-05

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 46.11  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 240 GRIVPEKGPHLAVEAARRTGLRLDLAGrVGDDR-YMERVLAPRLRDagdSVRYHGPLGRDALVPLVaSVAVALVTPCWE- 317
Cdd:cd03795   198 GRLVYYKGLDYLIEAAQYLNYPIVIGG-EGPLKpDLEAQIELNLLD---NVKFLGRVDDEEKVIYL-HLCDVFVFPSVLr 272

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1778635129 318 -EPFGLTAIEALACGTPVVA--LARGGIREILSGQPGVVlVEPGrDPAsALAASI 369
Cdd:cd03795   273 sEAFGIVLLEAMMCGKPVIStnIGTGVPYVNNNGETGLV-VPPK-DPD-ALAEAI 324
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 255-369 3.96e-05

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 45.42  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 255 ARRTGLRLDLAGRvGDDRYMERVLAPRLrDAGDSVRYhgpLGRDALVPLVASVAVALVTPCWEEPFGLTAIEALACGTPV 334
Cdd:cd04962   222 RRKIPAKLLLVGD-GPERVPAEELAREL-GVEDRVLF---LGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPV 296

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1778635129 335 VALARGGIREILS-GQPGvVLVEPGR-DPASALAASI 369
Cdd:cd04962   297 VSSNAGGIPEVVKhGETG-FLSDVGDvDAMAKSALSI 332
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 230-369 4.87e-05

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 45.03  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 230 PTDRPRAVWTGRIVPEKGPHLAVEAARRT----GLRLDLAGRvGDDRymERVLAPRLRDAGDSVRYHGPLGRDALVPLVA 305
Cdd:cd03794   214 LDDKFVVVYAGNIGKAQGLETLLEAAERLkrrpDIRFLFVGD-GDEK--ERLKELAKARGLDNVTFLGRVPKEEVPELLS 290

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778635129 306 SVAVALVTPCWEEPFGLTA----IEALACGTPVVALARGGIREILSGQPGVVLVEPGrDPAsALAASI 369
Cdd:cd03794   291 AADVGLVPLKDNPANRGSSpsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPG-DPE-ALADAI 356
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 232-374 9.96e-05

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 44.25  E-value: 9.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 232 DRPRAVWTGRIVPEKGPHLAVEAAR-----RTGLRLDLAGRV-GDDRYME--RVLAPRLRdAGDSVRYhgpLGRDALVPL 303
Cdd:cd03813   292 EPPVVGLVGRVVPIKDVKTFIRAFKlvrraMPDAEGWLIGPEdEDPEYAQecKRLVASLG-LENKVKF---LGFQNIKEY 367

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778635129 304 VASVAVALVTPCwEEPFGLTAIEALACGTPVVALARGGIREILSGQPGVV----LVEPGRDPaSALAASIPAALT 374
Cdd:cd03813   368 YPKLGLLVLTSI-SEGQPLVILEAMASGVPVVATDVGSCRELIYGADDALgqagLVVPPADP-EALAEALIKLLR 440
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 232-358 1.14e-04

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 44.32  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 232 DRPRAVWTGRIVPEKGPHLAVEA-ARRTGLRLDLagrVGDDRYMERvlaprLRD--AGDSVRYHGPLGRDALVPLVASVA 308
Cdd:PLN02871  262 EKPLIVYVGRLGAEKNLDFLKRVmERLPGARLAF---VGDGPYREE-----LEKmfAGTPTVFTGMLQGDELSQAYASGD 333

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1778635129 309 VaLVTPCWEEPFGLTAIEALACGTPVVALARGGIREILS-GQPGVV--LVEPG 358
Cdd:PLN02871  334 V-FVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIPpDQEGKTgfLYTPG 385
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 303-357 1.95e-04

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 43.62  E-value: 1.95e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1778635129  303 LVASVAVALVTPCWEEPFGLTAIEALACGTPVVALARGGIREILSGQPGVVLVEP 357
Cdd:TIGR02468  567 LAAKTKGVFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIHRVLDNGLLVDP 621
PLN00142 PLN00142
sucrose synthase
 310-346 5.16e-04

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 42.27  E-value: 5.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1778635129 310 ALVTPCWEEPFGLTAIEALACGTPVVALARGGIREIL 346
Cdd:PLN00142  669 AFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEII 705
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 250-357 7.72e-04

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 41.42  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 250 LAVEAAR--------RTGLRLDLAGRVgDDRYMERV--------LAPRLRDAGDSVRY-HGPLGRDALVPLVASVAVaLV 312
Cdd:cd03805   228 LAIEAFAklkqklpeFENVRLVIAGGY-DPRVAENVeyleelqrLAEELLNVEDQVLFlRSISDSQKEQLLSSALAL-LY 305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1778635129 313 TPCwEEPFGLTAIEALACGTPVVALARGGIRE-ILSGQPGvVLVEP 357
Cdd:cd03805   306 TPS-NEHFGIVPLEAMYAGKPVIACNSGGPLEtVVEGVTG-FLCEP 349
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 240-343 1.33e-03

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 40.62  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 240 GRIVPEKGPHLAVEAARR---TGLRLDLAGRvGDDRYmERVLAPRLRDAGDSVR----YHGPLGRdalvPLVASVAVALV 312
Cdd:cd03791   301 GRLTEQKGVDLILDALPElleEGGQLVVLGS-GDPEY-EQAFRELAERYPGKVAvvigFDEALAH----RIYAGADFFLM 374

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1778635129 313 tPCWEEPFGLTAIEALACGTPVVALARGGIR 343
Cdd:cd03791   375 -PSRFEPCGLVQMYAMRYGTLPIVRRTGGLA 404
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 316-361 4.15e-03

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 38.97  E-value: 4.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1778635129 316 WEEpFGLTAIEALACGTPVVALARGGIREILSGQPGVVlvePGRDP 361
Cdd:cd04951   272 WEG-FGLVVAEAMACERPVVATDAGGVAEVVGDHNYVV---PVSDP 313
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 235-336 7.39e-03

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 38.05  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778635129 235 RAVWTGRIVPEKGPHLAVEA---ARRT--GLRLDLAGRvGDDRYMERVLAPRLRdAGDSV---RYHGPLG---RDALVPL 303
Cdd:cd04949   162 KIITISRLAPEKQLDHLIEAvakAVKKvpEITLDIYGY-GEEREKLKKLIEELH-LEDNVflkGYHSNLDqeyQDAYLSL 239

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1778635129 304 VASVAvalvtpcweEPFGLTAIEALACGTPVVA 336
Cdd:cd04949   240 LTSQM---------EGFGLTLMEAIGHGLPVVS 263
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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